FK506-binding protein 4 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot Q06205 (FKBP4_YEAST)

Last modified November 24, 2009. Version 76. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    FK506-binding protein 4
    EC=5.2.1.8
Alternative name(s):
    Peptidyl-prolyl cis-trans isomerase
      Short name=PPIase
      Short name=Rotamase

Gene names

Name:	FPR4
Ordered Locus Names:	YLR449W
ORF Names:	L9324.3

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	392 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subunit structure	Interacts with NOP53. Ref.4
Subcellular location	Nucleus Potential.
Miscellaneous	Present with 14100 molecules/cell in log phase SD medium. Ref.3
Sequence similarities	Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily. Contains 1 PPIase FKBP-type domain.

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Ontologies

Keywords
Cellular component	Nucleus
Molecular function	Isomerase Rotamase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	chromatin silencing at rDNA Inferred from mutant phenotype. Source: SGD histone peptidyl-prolyl isomerization Inferred from direct assay. Source: SGD negative regulation of histone H3-K36 methylation Inferred from mutant phenotype. Source: SGD nucleosome assembly Inferred from direct assay. Source: SGD positive regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction. Source: SGD protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from direct assay. Source: SGD
Molecular function	histone binding Inferred from direct assay. Source: SGD macrolide binding Inferred from direct assay. Source: SGD peptidyl-prolyl cis-trans isomerase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
GAR1	P28007	1	EBI-6956,EBI-7321
HHF1	P02309	2	EBI-6956,EBI-8113
HHT1	P61830	2	EBI-6956,EBI-8098
LOC1	P43586	1	EBI-6956,EBI-22906
NOC2	P39744	1	EBI-6956,EBI-29259

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 392

392

FK506-binding protein 4

PRO_0000075314

Regions

Domain

306 – 392

PPIase FKBP-type

Compositional bias

191 – 199

Poly-Glu

Amino acid modifications

Modified residue

Phosphothreonine Ref.7

Modified residue

Phosphoserine Ref.7 Ref.2 Ref.5 Ref.6

Modified residue

Phosphoserine Ref.7 Ref.2 Ref.5 Ref.6

Modified residue

218

Phosphoserine Ref.7

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Sequences

Sequence

Length

Mass (Da)

Tools

Q06205-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: CF90C6714F04572E
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FASTA

392

43,903

        10         20         30         40         50         60 
MSDMLPLATY SLNVEPYSPT PALNFKIPVT IRITMAAIDP EPFDDDKKPS TLRIIKRNPE 

        70         80         90        100        110        120 
LTRGEYYNQD NNDGLEEDES ESEQEADVPK RSVKSKKGKA VEQSESEDSE DENEIDDEFE 

       130        140        150        160        170        180 
ECVLLTLSPK GQYQQALDIT IAPEEDVQFV VTGSYTISLT GNYVKHPFDN SSDSDEDEED 

       190        200        210        220        230        240 
YYSDEESSNG EEEEEEEEED DEELSSGDDD LDDLVDASDI ESRLDELVKK DEKKKNNKKD 

       250        260        270        280        290        300 
SKRKHEEDEE ESAKPAEKKQ TTKKDKKAEK VKDSEESKPK PKTKLLEGGI IIEDRVTGKG 

       310        320        330        340        350        360 
PHAKKGTRVG MRYVGKLKNG KVFDKNTKGK PFVFKLGQGE VIKGWDIGVA GMAVGGERRI 

       370        380        390 
VIPAPYAYGK QALPGIPANS ELTFDVKLVS MK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, MASS SPECTROMETRY.
[3]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[4]	"Nop53p is a novel nucleolar 60S ribosomal subunit biogenesis protein." Sydorskyy Y., Dilworth D.J., Halloran B., Yi E.C., Makhnevych T., Wozniak R.W., Aitchison J.D. Biochem. J. 388:819-826(2005) [PubMed: 15686447] [Abstract] Cited for: INTERACTION WITH NOP53, MASS SPECTROMETRY.
[5]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, MASS SPECTROMETRY.
[6]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, MASS SPECTROMETRY.
[7]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-80; SER-82 AND SER-218, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	U22382 Genomic DNA. Translation: AAB67528.1.
PIR	S55971.
RefSeq	NP_013554.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:909N.
IntAct	Q06205. 40 interactions.
STRING	Q06205.
Proteomic databases
PeptideAtlas	Q06205.
PRIDE	Q06205.
Genome annotation databases
Ensembl	YLR449W; YLR449W; YLR449W; Saccharomyces cerevisiae. [Genome view]
GeneID	851170.
KEGG	sce:YLR449W.
NMPDR	fig\|4932.3.peg.4585.
Organism-specific databases
CYGD	YLR449w.
SGD	S000004441. FPR4.
Phylogenomic databases
HOGENOM	Q06205.
OMA	DITIAPE
OrthoDB	EOG9PNZZZ
Enzyme and pathway databases
BRENDA	5.2.1.8. 250.
Gene expression databases
ArrayExpress	Q06205.
Genevestigator	Q06205.
GermOnline	YLR449W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001179. PPIase_FKBP. [Graphical view]
PANTHER	PTHR10516. PPIase_FKBP. 1 hit.
Pfam	PF00254. FKBP_C. 1 hit. [Graphical view]
PROSITE	PS50059. FKBP_PPIASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	967978.

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Entry information

Entry name

FKBP4_YEAST

Accession

Primary (citable) accession number: Q06205

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1996
Last modified:	November 24, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents